Recombinant Human Receptor-interacting serine/threonine-protein kinase 1 (RIPK1), partial

Cell death protein RIP Receptor-interacting protein 1 Short name: RIP-1 Serine/threonine-protein kinase RIP RIP, RIP1

Baculovirus

MQPDMSLNVIKMKSSDFLESAELDSGGFGKVSLCF HRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRL RHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLK AEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLK PENILVDNDFHIKIADLGLASFKMWSKLNNEEHNE LREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSD VYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGN RPDVDDITEYCPREIISLMKLCWEANPEARPTFPG IEEKFRPFYLSQLEESVEEDVKSLKKEYSNENAVV KRMQSLQLDCVAVPSSRSNSATEQPGSLHSSQGLG MGPVEESWFAPSLEHPQEENEPSLQ

N-terminal 10xHis-tagged and C-terminal Myc-tagged

>85% as determined by SDS-PAGE.

Not tested

Ice packs

1 year

Serine-threonine kinase which transduces inflammatory and cell-death signals (programmed necrosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade. Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules. Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation. Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death. RIPK1 and RIPK3 association, in particular, forms a necrosis-inducing complex.

Cytoplasm, Cell membrane

NF-kappaBsignalingpathway